Evidence map›Paper›PMID 24252639›Full record

ReviewChemistry and physics of lipids2014

Structural transformations of cytochrome c upon interaction with cardiolipin.

Julia Muenzner, Ekaterina V Pletneva

Abstract readReview
In one paragraph

Review in Chemistry and physics of lipids, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Increase in the Peroxidase Activity of the CytochromeInternational journal of molecular sciences · 2024
    Article
  7. Composition of the CytochromeMolecules (Basel, Switzerland) · 2023
    Article
  8. The role of mitochondria in rheumatic diseases.Nature reviews. Rheumatology · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Binding of S. cerevisiae iso-1 cytochrome c and its surface lysine-to-alanine variants to cardiolipin: charge effects and the role of the lipid to protein ratio.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Julia MuenznerDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, United States.
Ekaterina V PletnevaDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, United States. Electronic address: ekaterina.pletneva@dartmouth.edu.
Dartmouth College · US

Funding

Conformational Properties of Cytochromes in DiseaseR01GM098502 · NIGMS · DARTMOUTH COLLEGE · PI PLETNEVA, EKATERINA · 2011 to 2023
$2.9M
NIGMS NIH HHS R01 GM098502
6 · The paper itself

Abstract

Interactions of cytochrome c (cyt c) with cardiolipin (CL) play a critical role in early stages of apoptosis. Upon binding to CL, cyt c undergoes changes in secondary and tertiary structure that lead to a dramatic increase in its peroxidase activity. Insertion of the protein into membranes, insertion of CL acyl chains into the protein interior, and extensive unfolding of cyt c after adsorption to the membrane have been proposed as possible modes for interaction of cyt c with CL. Dissociation of Met80 is accompanied by opening of the heme crevice and binding of another heme ligand. Fluorescence studies have revealed conformational heterogeneity of the lipid-bound protein ensemble with distinct polypeptide conformations that vary in the degree of protein unfolding. We correlate these recent findings to other biophysical observations and rationalize the role of experimental conditions in defining conformational properties and peroxidase activity of the cyt c ensemble. Latest time-resolved studies propose the trigger and the sequence of cardiolipin-induced structural transitions of cyt c.

Indexed as

AnimalsCardiolipinsCell Membrane PermeabilityCytochromes cFree RadicalsHemeHumansProtein BindingCardiolipinsCytochromes cFree RadicalsHemeApoptosisHemePeroxidaseProtein folding

Identifiers

PMID24252639
PMCPMC3979421
OpenAlexW2049774523

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.